Monthly Archives: November 2015

Direct visualisation of PLCη2-LIMK1 interactions (red dots) in Neuro2A cells within growing neurites using a proximity ligand assay. Interactions can also be seen in the cell body and nucleus (stained blue).

Phosphatidylinositol (PhoIns)-specific phospholipase C enzymes (PLCs) are central to the inositol lipid signalling pathways and contribute to intracellular Ca2+ release and protein kinase C activation in mammalian neurons. Six distinct classes of PhoIns-specific PLCs are known to exist in mammals (β, γ, δ, ε, ζ, and η), all of which are activated by distinct membrane receptor-mediated events. The Stewart lab previously revealed that expression of the PLC isozyme, PLC-η2 is essential for neurite growth, a process central to normal neuronal differentiation. A new study from the lab has gone a step further and shown that active PLC-η2 is needed for neurite growth to occur. Furthermore, the study also revealed that PLC-η2 interacts directly with LIM Domain Kinase 1, a key cytoskeletal regulatory protein previously implicated in this process. The new findings are published in the journal, Histochemistry and Cell Biology. Full text is available here: DOI 10.1007/s00418-015-1390-7.